Mössbauer studies of beef heart aconitase: evidence for facile interconversions of iron-sulfur clusters.
Beef heart aconitase, isolated under aerobic conditions, has been studied with Mössbauer and EPR spectroscopy. In the oxidized state, the enzyme exhibits an EPR signal at g = 2.01. The Mössbauer data show that this signal is associated with a 3Fe cluster. In dithionite-reduced aconitase, the 3Fe clu...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1982
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC345907/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6280166/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.79.4.1096 |
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